Critical Review of Mass Spectrometry of Protein Analysis
Mass spectrometry is an analytical technique that measures different the mass by quantifying the mass to charge ratio (m/z) of charged particles. The use of this method can be for determining masses of particles, determining element configuration, identifying unknown compounds of a molecule and for defining molecule’s structures by stating the isotopic composition and observing its fragmentations.1
The generation of charged molecules is derived by the activation of the loss or gain charges as it is easier to manipulate than the neutral ones. However, it is prominently used also for determining neutral masses but more ...view middle of the document...
The data analysis of mass spectrometry is very specific to the type of experiment
Mass Spectrometry and Proteomics
Mass Spectrometry (MS) allows experts to identify and measure proteins in a biological composition matrix. The technique is very accurate at individualising proteins that have a differentiation even in the smallest atom. However, this technology is yet not established to separate composition mixtures from natural human bio-specimens proteins4.
Proteomics or proteome is the study of proteins which consist of identifying and classification of proteins specified in a single cell or tissue at a particular point of time.
Before Mass Spectrometric detection there are two main priority methods to be mentioned, helping on the determination of protein complexes of a cell or tissue. One is the multi-dimensional chromatography where the proteins are divided relating to the ionic attractiveness, molecular identity and size via ion exchange, molecular segregation, affinity and reverse-phase chromatography. Subsequently, these proteins or their products are introduced into Electrospray Ionization (ESI) which is a fraction based on mass spectrometry, distinguishing the molecular weight and the categorisations of the protein.
The second method used to investigate proteins is the two- dimensional gel electrophoresis in order to distinct and validate them. The first step in this process is the distinction of the cell or tissue referring to the charge and the size5. The proteins are absorbed in gel to discharge the peptides.
The components can be examined by either the ESI or MALDI-based mass spectrometer (matrix-assisted laser desorption/ionization).
In mass spectrometry samples are often entranced via a direct attachment probe or a capillary column for Electron Ionization, Electrospray Ionization with Gas Chromatography (GC) or the sample plate for MALDI.
With every method there are advantages and disadvantages to be aware that makes it stand out.
Ionization methods allow many compounds to accept the proton, cation or deprotonation to become ionized, however some of these compounds are not stable or cannot accept protons easily. The composites can be very particular and often can generate much fragmentation, resulting in unclear results whether it is a molecular ion or a fragment.
Opportunities for additional developments of Proteomic Analysis
Considering the importance of proteomics many studies have been searched to improve the evaluation and identification of specificity in genetic diagnoses.
As mentioned before MS-based methods give a configuration recognition which use protein ionization produced through cells...